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Database: UniProt
Entry: A5JSI3_STRSU
LinkDB: A5JSI3_STRSU
Original site: A5JSI3_STRSU 
ID   A5JSI3_STRSU            Unreviewed;      1035 AA.
AC   A5JSI3;
DT   26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Cell wall hydrolase/autolysin {ECO:0000313|EMBL:ABQ42871.1};
DE   Flags: Fragment;
OS   Streptococcus suis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1307 {ECO:0000313|EMBL:ABQ42871.1};
RN   [1] {ECO:0000313|EMBL:ABQ42871.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=260 {ECO:0000313|EMBL:ABQ42871.1};
RA   Gu H., Lu C.;
RT   "Newly identified complete ivi genes of Streptococcus suis serotype 2.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; EF563969; ABQ42871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5JSI3; -.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3760; -; 6.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR013688; GBS_Bsp-like.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF08481; GBS_Bsp-like; 6.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABQ42871.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..1035
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038806098"
FT   DOMAIN          896..1026
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          152..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..237
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABQ42871.1"
SQ   SEQUENCE   1035 AA;  113129 MW;  3D668A354E43E31E CRC64;
     LFLHVKYIKE MFVKKRTLLF LSLCASALNA QLVQADMVNA PSSQVSSSQV AETGGQLSVV
     DEAGQIKAIL SNIQGEIIGV TAQFSSETNS GITVTFSMDE QGRYVAVLDR SAFAEEDQVF
     SLKLTAQLTD GSFQTLSDYS FEWKKDVVSA AEKPTALDNS DATPSKIEEE ATSTTTSSTV
     NSSLTAGATS STSNSLTRSS SNTIAGSSNG STSVPSARVS TASSSVNVTQ PTGTITIENR
     NDAQGTFDVR VTNVSSPKDI SSVILPTWSQ TDDLRWYEAT RQSDGSYKLT VNKKDHKYRT
     GTYTVHLYYK DSSGGLTGAG GTTTHLSEAK PTGTITIENR NDAQGTFDVR VTNVSSPKDI
     SSVILPTWSQ TDDLRWYEAT RQSDGSYKLT VNKKDHKYRT GTYTVHLYYK DSSGGLTGAG
     GTTTHLSEVK PTGTITIENR NDAQGTFDVR VTNVSSPKDI ASVLLPTWSQ SDDIRWYEAT
     RQSDGSYKLT VNKKGHKYRT GTYTVHLYYK DSNGGLTGAG GTTTHLSEAK PTGTITIENR
     NDAQGTFDVR VTNVSSPKDI ASVLLPTWSQ SDDIRWYEAT RQSDGSYKLT VNKKDHKYRT
     GTYTVHLYYK DSNGGLTGAG GTTTHLSEAK PTGTITIENR NDAQGTFDVR VTNVSSPKDI
     ASVLLPTWSQ SDDIRWYEAT RQSDGSYKLT VNKKDHKYRT GTYTVHLYYK DSNGGLTGAG
     GTTTHLSEAK PTGTITIENR NDAQGTFDVR VTNVSSPKDI ASVLLPTWSQ SDDIRWYEAT
     RQSDGSYKLT VNKKDHKYRT GTYTVHLYYK DSNGGLTGAG GTTTHLSNPS AQRSYTVYID
     PGHGGRDSGA SYGGVHEKNL ALSVSNKLRE NLLQYGINVL MTRTGDYDVD FKTERSRMTN
     ASNADLFISI HFNATGAGVS NATGIETYWY QYNPEYQPKI NKEMHNNPTR LAESEILANK
     VQESLIKETG AVNRGVRRET FAVLRETAIP AILVELGFMD NPSELQVIKQ DSYHTRLAKA
     LAQGVMNWYG AVEGK
//
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